1f7t

HOLO-(ACYL CARRIER PROTEIN) SYNTHASE AT 1.8A


Structural alignment of the structures of the B. subtilis AcpS trimer (1f7t, in red, cyan , and yellow ) the Mtb AcpS trimer (in lime , blue , and orange ) and the Mycobacterium tuberculosis (Mtb) AcpS trimer (3hqj, in lime , blue , and orange ) reveals that the Mtb AcpS structure is similar to those of other members of group I phosphopantetheine transferase (PPT) family. The important difference is that the extended α3 helix of Mtb AcpS has open conformation. Such open conformation permits to the extended loop of one monomer (lime ) to interact with adjacent monomer (blue ). The considerably shorter α3 of one B. subtilis AcpS monomer (red ) has closed conformation and this doesn't allow interaction with the neighboring monomer (cyan ).

About this Structure
1F7T is a 6 chains structure of sequences from Bacillus subtilis. Full crystallographic information is available from OCA.